HEADER IMMUNE SYSTEM 11-DEC-23 8REK TITLE PLASMODIUM VIVAX APICAL MEMBRANE ANTIGEN 1/FAB COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: APICAL MEMBRANE ANTIGEN 1 (FRAGMENT); COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: FAB 8.1.1 HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: FAB 8.1.1 LIGHT CHAIN; COMPND 11 CHAIN: L SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM VIVAX SAL-1; SOURCE 3 ORGANISM_TAXID: 126793; SOURCE 4 GENE: AMA-1; SOURCE 5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 9 ORGANISM_TAXID: 10090; SOURCE 10 MOL_ID: 3; SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 12 ORGANISM_TAXID: 10090 KEYWDS AMA-1, PLASMODIUM VIVAX, ANTIGEN, FAB, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR G.A.BENTLEY,F.A.SAUL,B.VULLIEZ-LENORMAND REVDAT 1 16-OCT-24 8REK 0 JRNL AUTH F.A.SAUL,B.VULLIEZ-LE NORMAND,A.BOES,H.SPIEGEL,C.H.M.KOCKEN, JRNL AUTH 2 B.W.FABER,G.A.BENTLEY JRNL TITL CONFORMATIONAL VARIABILITY IN THE D2 LOOP OF PLASMODIUM JRNL TITL 2 APICAL MEMBRANE ANTIGEN 1. JRNL REF J STRUCT BIOL X V. 10 00110 2024 JRNL REFN ESSN 2590-1524 JRNL PMID 39324028 JRNL DOI 10.1016/J.YJSBX.2024.100110 REMARK 2 REMARK 2 RESOLUTION. 3.05 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0415 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.05 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.54 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 17069 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.225 REMARK 3 R VALUE (WORKING SET) : 0.221 REMARK 3 FREE R VALUE : 0.292 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300 REMARK 3 FREE R VALUE TEST SET COUNT : 946 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.05 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.13 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1229 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.3810 REMARK 3 BIN FREE R VALUE SET COUNT : 71 REMARK 3 BIN FREE R VALUE : 0.3860 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6293 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 95.22 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.76000 REMARK 3 B22 (A**2) : 0.41000 REMARK 3 B33 (A**2) : 0.35000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.551 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.513 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 68.080 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.912 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.866 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6450 ; 0.021 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 5781 ; 0.017 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8770 ; 1.646 ; 1.660 REMARK 3 BOND ANGLES OTHERS (DEGREES): 13361 ; 0.787 ; 1.574 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 807 ; 6.666 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 32 ; 3.302 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1015 ;13.615 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 960 ; 0.086 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7621 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1471 ; 0.004 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3258 ; 3.616 ; 5.873 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3258 ; 3.615 ; 5.873 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4055 ; 5.814 ;10.715 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4056 ; 5.818 ;10.717 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3192 ; 3.346 ; 6.043 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3193 ; 3.346 ; 6.045 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4716 ; 5.545 ;11.144 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6217 ; 8.205 ;55.090 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6218 ; 8.205 ;55.100 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 44 A 474 REMARK 3 ORIGIN FOR THE GROUP (A): -25.7772 -11.3862 12.4774 REMARK 3 T TENSOR REMARK 3 T11: 0.0577 T22: 0.0862 REMARK 3 T33: 0.0872 T12: 0.0452 REMARK 3 T13: -0.0463 T23: -0.0320 REMARK 3 L TENSOR REMARK 3 L11: 3.1191 L22: 4.4840 REMARK 3 L33: 2.5960 L12: 1.1831 REMARK 3 L13: -1.5270 L23: -1.4668 REMARK 3 S TENSOR REMARK 3 S11: 0.0287 S12: -0.2144 S13: -0.3167 REMARK 3 S21: 0.1223 S22: -0.0714 S23: 0.0514 REMARK 3 S31: 0.1318 S32: 0.0636 S33: 0.0426 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 1 H 114 REMARK 3 RESIDUE RANGE : L 1 L 107 REMARK 3 ORIGIN FOR THE GROUP (A): -0.2928 26.7779 -9.1975 REMARK 3 T TENSOR REMARK 3 T11: 0.3279 T22: 0.2209 REMARK 3 T33: 0.1179 T12: 0.0675 REMARK 3 T13: 0.1273 T23: 0.0821 REMARK 3 L TENSOR REMARK 3 L11: 2.9056 L22: 4.8722 REMARK 3 L33: 3.0472 L12: 0.6867 REMARK 3 L13: -0.0234 L23: 1.0243 REMARK 3 S TENSOR REMARK 3 S11: -0.1320 S12: 0.2743 S13: 0.2503 REMARK 3 S21: -0.4275 S22: 0.1446 S23: -0.2525 REMARK 3 S31: -0.3991 S32: 0.0885 S33: -0.0126 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 115 H 213 REMARK 3 RESIDUE RANGE : L 108 L 211 REMARK 3 ORIGIN FOR THE GROUP (A): 19.4661 53.1877 -14.5111 REMARK 3 T TENSOR REMARK 3 T11: 0.5929 T22: 0.3852 REMARK 3 T33: 0.9862 T12: 0.1173 REMARK 3 T13: 0.1846 T23: 0.1035 REMARK 3 L TENSOR REMARK 3 L11: 1.7713 L22: 2.3986 REMARK 3 L33: 3.4987 L12: 1.6297 REMARK 3 L13: 0.1671 L23: -0.4795 REMARK 3 S TENSOR REMARK 3 S11: -0.0359 S12: 0.0450 S13: 0.1336 REMARK 3 S21: -0.1954 S22: -0.1227 S23: -0.7743 REMARK 3 S31: 0.2177 S32: 0.5757 S33: 0.1586 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 8REK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-DEC-23. REMARK 100 THE DEPOSITION ID IS D_1292134437. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-SEP-06 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.934 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18062 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050 REMARK 200 RESOLUTION RANGE LOW (A) : 73.390 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 7.100 REMARK 200 R MERGE (I) : 0.16700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.26 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 7.20 REMARK 200 R MERGE FOR SHELL (I) : 1.20300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE OBTAINED BY MIXING 0.8 REMARK 280 MICRO-L OF PVAMA1-FAB COMPLEX WITH 0.2 MICRO-L OF 15% 1,2,3 REMARK 280 HEPTANETRIOL AND 0.8 MICRO-L OF RESERVOIR BUFFER COMPRISING 20% REMARK 280 PEG 2000 MONOMETHYLETHER AND 0.1 M TRIS PH 7. THE FINAL PROTEIN REMARK 280 CONCENTRATION WAS 3.2 MG/ML., VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 290K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 36.69500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 107.34000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.69500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 107.34000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4780 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 37440 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER A 41 REMARK 465 ILE A 42 REMARK 465 PRO A 43 REMARK 465 MET A 171 REMARK 465 ALA A 172 REMARK 465 GLY A 173 REMARK 465 ASP A 174 REMARK 465 GLN A 175 REMARK 465 ASN A 176 REMARK 465 ALA A 212 REMARK 465 GLN A 213 REMARK 465 ASN A 214 REMARK 465 ARG A 215 REMARK 465 ASP A 216 REMARK 465 PRO A 295 REMARK 465 THR A 296 REMARK 465 GLN A 297 REMARK 465 TYR A 298 REMARK 465 GLU A 299 REMARK 465 GLU A 300 REMARK 465 GLU A 301 REMARK 465 MET A 302 REMARK 465 THR A 303 REMARK 465 ASP A 304 REMARK 465 TYR A 305 REMARK 465 GLN A 306 REMARK 465 GLY A 328 REMARK 465 ALA A 329 REMARK 465 PHE A 330 REMARK 465 ASN A 331 REMARK 465 SER A 332 REMARK 465 ARG A 404 REMARK 465 ASN A 405 REMARK 465 MET A 406 REMARK 465 ASN A 407 REMARK 465 LEU A 408 REMARK 465 TYR A 409 REMARK 465 GLU A 475 REMARK 465 ASN A 476 REMARK 465 GLY A 477 REMARK 465 GLU A 478 REMARK 465 GLU A 479 REMARK 465 LYS A 480 REMARK 465 SER A 481 REMARK 465 ASN A 482 REMARK 465 LYS A 483 REMARK 465 GLN A 484 REMARK 465 MET A 485 REMARK 465 LEU A 486 REMARK 465 LEU A 487 REMARK 465 LEU A 488 REMARK 465 GLU A 489 REMARK 465 GLN A 490 REMARK 465 LYS A 491 REMARK 465 LEU A 492 REMARK 465 ILE A 493 REMARK 465 SER A 494 REMARK 465 GLU A 495 REMARK 465 GLU A 496 REMARK 465 ASP A 497 REMARK 465 LEU A 498 REMARK 465 ASN A 499 REMARK 465 SER A 500 REMARK 465 ALA A 501 REMARK 465 VAL A 502 REMARK 465 ASP A 503 REMARK 465 HIS A 504 REMARK 465 HIS A 505 REMARK 465 HIS A 506 REMARK 465 HIS A 507 REMARK 465 HIS A 508 REMARK 465 HIS A 509 REMARK 465 GLY H 127 REMARK 465 CYS H 128 REMARK 465 GLY H 129 REMARK 465 ASP H 130 REMARK 465 THR H 131 REMARK 465 THR H 132 REMARK 465 GLY H 133 REMARK 465 SER H 134 REMARK 465 SER H 156 REMARK 465 GLY H 157 REMARK 465 SER H 158 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG A 112 CD NE CZ NH1 NH2 REMARK 470 LYS A 120 CG CD CE NZ REMARK 470 LYS A 122 CD CE NZ REMARK 470 LYS A 148 CG CD CE NZ REMARK 470 ARG A 206 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 312 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 317 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 392 CG CD CE NZ REMARK 470 LYS A 400 CG CD CE NZ REMARK 470 LYS A 401 CG CD CE NZ REMARK 470 ARG A 415 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 431 CG CD CE NZ REMARK 470 ARG A 438 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 459 CG CD CE NZ REMARK 470 LYS H 13 CG CD CE NZ REMARK 470 TYR H 56 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS H 75 CG CD CE NZ REMARK 470 GLN H 97 CG CD OE1 NE2 REMARK 470 LYS H 143 CG CD CE NZ REMARK 470 GLN H 171 CG CD OE1 NE2 REMARK 470 LYS H 209 CG CD CE NZ REMARK 470 LEU H 210 CG CD1 CD2 REMARK 470 ARG L 77 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 147 CG CD CE NZ REMARK 470 LYS L 169 CG CD CE NZ REMARK 470 LYS L 183 CG CD CE NZ REMARK 470 LYS L 199 CG CD CE NZ REMARK 470 LYS L 207 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 HIS A 68 CG HIS A 68 CD2 -0.120 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 76 57.99 -145.85 REMARK 500 GLU A 83 -68.56 78.42 REMARK 500 ASN A 84 -58.87 -142.58 REMARK 500 GLN A 119 88.72 -67.99 REMARK 500 ASN A 132 -44.89 -141.69 REMARK 500 ASP A 133 58.23 87.47 REMARK 500 TYR A 147 48.72 -99.28 REMARK 500 ALA A 167 44.09 -97.46 REMARK 500 GLN A 200 -47.93 -135.35 REMARK 500 ASN A 202 86.01 -158.05 REMARK 500 MET A 203 51.08 -141.59 REMARK 500 TYR A 207 76.27 -116.29 REMARK 500 CYS A 208 -39.94 -167.56 REMARK 500 ASP A 242 35.71 -93.04 REMARK 500 ARG A 249 -71.25 -127.02 REMARK 500 VAL A 261 69.04 -115.41 REMARK 500 ASP A 262 82.10 64.01 REMARK 500 ASP A 293 51.70 -105.23 REMARK 500 PHE A 335 67.25 -118.33 REMARK 500 GLN A 380 -42.11 -157.69 REMARK 500 ILE A 399 55.74 -95.15 REMARK 500 ASP A 412 -65.03 -145.40 REMARK 500 LYS A 459 -162.10 -77.76 REMARK 500 LYS H 43 55.43 76.58 REMARK 500 ASN H 76 74.59 39.74 REMARK 500 SER H 162 61.07 -105.70 REMARK 500 SER H 172 69.21 -163.93 REMARK 500 THR H 187 38.93 -87.55 REMARK 500 SER H 203 57.29 73.81 REMARK 500 ALA L 50 67.16 71.57 REMARK 500 THR L 51 -73.30 73.03 REMARK 500 SER L 72 114.28 -160.53 REMARK 500 ALA L 83 93.58 -54.73 REMARK 500 TRP L 91 49.94 -145.98 REMARK 500 ASP L 110 87.66 -65.95 REMARK 500 SER L 116 95.48 -162.43 REMARK 500 SER L 127 72.93 -152.69 REMARK 500 ASN L 138 83.13 63.17 REMARK 500 ILE L 144 113.83 -161.49 REMARK 500 GLN L 156 -46.06 81.78 REMARK 500 SER L 171 42.31 94.58 REMARK 500 ASN L 190 -58.13 -120.99 REMARK 500 THR L 202 -60.95 98.56 REMARK 500 LYS L 207 105.35 -162.31 REMARK 500 REMARK 500 REMARK: NULL DBREF 8REK A 43 487 UNP Q9TY14 Q9TY14_PLAVI 1 445 DBREF 8REK H 1 213 PDB 8REK 8REK 1 213 DBREF 8REK L 1 214 PDB 8REK 8REK 1 214 SEQADV 8REK SER A 41 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK ILE A 42 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK ASN A 178 UNP Q9TY14 SER 136 ENGINEERED MUTATION SEQADV 8REK ASP A 226 UNP Q9TY14 ASN 184 ENGINEERED MUTATION SEQADV 8REK GLN A 441 UNP Q9TY14 ASN 399 ENGINEERED MUTATION SEQADV 8REK LEU A 488 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK GLU A 489 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK GLN A 490 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK LYS A 491 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK LEU A 492 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK ILE A 493 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK SER A 494 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK GLU A 495 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK GLU A 496 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK ASP A 497 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK LEU A 498 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK ASN A 499 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK SER A 500 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK ALA A 501 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK VAL A 502 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK ASP A 503 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK HIS A 504 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK HIS A 505 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK HIS A 506 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK HIS A 507 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK HIS A 508 UNP Q9TY14 EXPRESSION TAG SEQADV 8REK HIS A 509 UNP Q9TY14 EXPRESSION TAG SEQRES 1 A 469 SER ILE PRO THR VAL GLU ARG SER THR ARG MET GLY ASN SEQRES 2 A 469 PRO TRP LYS ALA PHE MET GLU LYS TYR ASP ILE GLU ARG SEQRES 3 A 469 THR HIS SER SER GLY VAL ARG VAL ASP LEU GLY GLU ASP SEQRES 4 A 469 ALA GLU VAL GLU ASN ALA LYS TYR ARG ILE PRO ALA GLY SEQRES 5 A 469 ARG CYS PRO VAL PHE GLY LYS GLY ILE VAL ILE GLU ASN SEQRES 6 A 469 SER ASP VAL SER PHE LEU ARG PRO VAL ALA THR GLY ASP SEQRES 7 A 469 GLN LYS LEU LYS ASP GLY GLY PHE ALA PHE PRO ASN ALA SEQRES 8 A 469 ASN ASP HIS ILE SER PRO MET THR LEU ALA ASN LEU LYS SEQRES 9 A 469 GLU ARG TYR LYS ASP ASN VAL GLU MET MET LYS LEU ASN SEQRES 10 A 469 ASP ILE ALA LEU CYS ARG THR HIS ALA ALA SER PHE VAL SEQRES 11 A 469 MET ALA GLY ASP GLN ASN SER ASN TYR ARG HIS PRO ALA SEQRES 12 A 469 VAL TYR ASP GLU LYS GLU LYS THR CYS HIS MET LEU TYR SEQRES 13 A 469 LEU SER ALA GLN GLU ASN MET GLY PRO ARG TYR CYS SER SEQRES 14 A 469 PRO ASP ALA GLN ASN ARG ASP ALA VAL PHE CYS PHE LYS SEQRES 15 A 469 PRO ASP LYS ASP GLU SER PHE GLU ASN LEU VAL TYR LEU SEQRES 16 A 469 SER LYS ASN VAL ARG ASN ASP TRP ASP LYS LYS CYS PRO SEQRES 17 A 469 ARG LYS ASN LEU GLY ASN ALA LYS PHE GLY LEU TRP VAL SEQRES 18 A 469 ASP GLY ASN CYS GLU GLU ILE PRO TYR VAL LYS GLU VAL SEQRES 19 A 469 GLU ALA GLU ASP LEU ARG GLU CYS ASN ARG ILE VAL PHE SEQRES 20 A 469 GLY ALA SER ALA SER ASP GLN PRO THR GLN TYR GLU GLU SEQRES 21 A 469 GLU MET THR ASP TYR GLN LYS ILE GLN GLN GLY PHE ARG SEQRES 22 A 469 GLN ASN ASN ARG GLU MET ILE LYS SER ALA PHE LEU PRO SEQRES 23 A 469 VAL GLY ALA PHE ASN SER ASP ASN PHE LYS SER LYS GLY SEQRES 24 A 469 ARG GLY PHE ASN TRP ALA ASN PHE ASP SER VAL LYS LYS SEQRES 25 A 469 LYS CYS TYR ILE PHE ASN THR LYS PRO THR CYS LEU ILE SEQRES 26 A 469 ASN ASP LYS ASN PHE ILE ALA THR THR ALA LEU SER HIS SEQRES 27 A 469 PRO GLN GLU VAL ASP LEU GLU PHE PRO CYS SER ILE TYR SEQRES 28 A 469 LYS ASP GLU ILE GLU ARG GLU ILE LYS LYS GLN SER ARG SEQRES 29 A 469 ASN MET ASN LEU TYR SER VAL ASP GLY GLU ARG ILE VAL SEQRES 30 A 469 LEU PRO ARG ILE PHE ILE SER ASN ASP LYS GLU SER ILE SEQRES 31 A 469 LYS CYS PRO CYS GLU PRO GLU ARG ILE SER GLN SER THR SEQRES 32 A 469 CYS ASN PHE TYR VAL CYS ASN CYS VAL GLU LYS ARG ALA SEQRES 33 A 469 GLU ILE LYS GLU ASN ASN GLN VAL VAL ILE LYS GLU GLU SEQRES 34 A 469 PHE ARG ASN TYR TYR GLU ASN GLY GLU GLU LYS SER ASN SEQRES 35 A 469 LYS GLN MET LEU LEU LEU GLU GLN LYS LEU ILE SER GLU SEQRES 36 A 469 GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS HIS SEQRES 37 A 469 HIS SEQRES 1 H 220 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 220 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 220 PHE THR PHE SER ASP TYR TYR MET TYR TRP VAL ARG GLN SEQRES 4 H 220 THR PRO GLU LYS ARG LEU GLU TRP VAL ALA THR ILE ASN SEQRES 5 H 220 ASP GLY GLY THR TYR THR TYR TYR PRO ASP SER VAL LYS SEQRES 6 H 220 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN ASN SEQRES 7 H 220 LEU TYR LEU GLN MET SER SER LEU LYS SER GLU ASP THR SEQRES 8 H 220 ALA MET TYR PHE CYS ALA ARG GLY SER GLN LEU GLY ARG SEQRES 9 H 220 GLY GLU PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 H 220 VAL SER ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO SEQRES 11 H 220 LEU ALA PRO GLY CYS GLY ASP THR THR GLY SER SER VAL SEQRES 12 H 220 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SER SEQRES 13 H 220 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER SER SEQRES 14 H 220 VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU TYR SEQRES 15 H 220 THR MET SER SER SER VAL THR VAL PRO SER SER THR TRP SEQRES 16 H 220 PRO SER GLN THR VAL THR CYS SER VAL ALA HIS PRO ALA SEQRES 17 H 220 SER SER THR THR VAL ASP LYS LYS LEU GLU PRO SER SEQRES 1 L 213 PCA ILE VAL LEU SER GLN SER PRO ALA ILE LEU SER ALA SEQRES 2 L 213 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER SEQRES 3 L 213 SER SER VAL SER TYR MET HIS TRP TYR GLN GLN LYS PRO SEQRES 4 L 213 GLY SER SER PRO LYS PRO TRP ILE TYR ALA THR PHE ASN SEQRES 5 L 213 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 L 213 SER GLY THR SER TYR SER LEU THR ILE SER ARG VAL GLU SEQRES 7 L 213 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TRP SER SEQRES 8 L 213 SER ASN PRO PRO THR PHE GLY ALA GLY THR LYS LEU GLU SEQRES 9 L 213 LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE SEQRES 10 L 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER SEQRES 11 L 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE SEQRES 12 L 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN SEQRES 13 L 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SEQRES 14 L 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS SEQRES 15 L 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA SEQRES 16 L 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE SEQRES 17 L 213 ASN ARG ASN GLU CYS HET PCA L 1 8 HETNAM PCA PYROGLUTAMIC ACID FORMUL 3 PCA C5 H7 N O3 HELIX 1 AA1 MET A 59 TYR A 62 5 4 HELIX 2 AA2 ASP A 63 HIS A 68 1 6 HELIX 3 AA3 THR A 139 TYR A 147 1 9 HELIX 4 AA4 ASN A 150 LYS A 155 1 6 HELIX 5 AA5 ASN A 157 ALA A 167 1 11 HELIX 6 AA6 ASP A 226 GLU A 230 5 5 HELIX 7 AA7 ASP A 242 CYS A 247 1 6 HELIX 8 AA8 ASP A 278 SER A 290 1 13 HELIX 9 AA9 ILE A 308 ARG A 313 1 6 HELIX 10 AB1 ASN A 316 SER A 322 1 7 HELIX 11 AB2 SER A 389 GLU A 398 1 10 HELIX 12 AB3 GLU A 460 ASN A 462 5 3 HELIX 13 AB4 GLU A 468 ARG A 471 5 4 HELIX 14 AB5 THR H 28 TYR H 32 5 5 HELIX 15 AB6 PRO H 60 LYS H 64 5 5 HELIX 16 AB7 ASN H 73 LYS H 75 5 3 HELIX 17 AB8 LYS H 83 THR H 87 5 5 HELIX 18 AB9 LEU H 159 SER H 161 5 3 HELIX 19 AC1 PRO H 184 TRP H 188 5 5 HELIX 20 AC2 GLU L 79 ALA L 83 5 5 HELIX 21 AC3 SER L 121 SER L 127 1 7 HELIX 22 AC4 LYS L 183 ARG L 188 1 6 SHEET 1 AA1 2 VAL A 45 ARG A 47 0 SHEET 2 AA1 2 ILE A 416 LEU A 418 1 O LEU A 418 N GLU A 46 SHEET 1 AA2 2 GLU A 78 GLU A 81 0 SHEET 2 AA2 2 LYS A 86 ILE A 89 -1 O TYR A 87 N ALA A 80 SHEET 1 AA3 4 VAL A 96 PHE A 97 0 SHEET 2 AA3 4 VAL A 233 LEU A 235 -1 O TYR A 234 N VAL A 96 SHEET 3 AA3 4 ALA A 183 ASP A 186 -1 N ALA A 183 O LEU A 235 SHEET 4 AA3 4 THR A 191 MET A 194 -1 O HIS A 193 N VAL A 184 SHEET 1 AA4 2 GLY A 100 ILE A 103 0 SHEET 2 AA4 2 PHE A 221 ASP A 224 -1 O LYS A 222 N VAL A 102 SHEET 1 AA5 6 LYS A 272 GLU A 275 0 SHEET 2 AA5 6 LYS A 353 PHE A 357 -1 O ILE A 356 N LYS A 272 SHEET 3 AA5 6 TRP A 344 ASP A 348 -1 N ASP A 348 O LYS A 353 SHEET 4 AA5 6 PHE A 370 THR A 374 -1 O THR A 373 N ALA A 345 SHEET 5 AA5 6 ASN A 251 GLY A 253 -1 N LEU A 252 O ALA A 372 SHEET 6 AA5 6 VAL A 382 ASP A 383 1 O ASP A 383 N ASN A 251 SHEET 1 AA6 3 CYS A 265 GLU A 266 0 SHEET 2 AA6 3 LYS A 256 TRP A 260 -1 N LEU A 259 O GLU A 266 SHEET 3 AA6 3 CYS A 363 ILE A 365 -1 O ILE A 365 N LYS A 256 SHEET 1 AA7 3 ILE A 423 SER A 424 0 SHEET 2 AA7 3 TYR A 447 VAL A 448 -1 O TYR A 447 N SER A 424 SHEET 3 AA7 3 GLU A 437 ARG A 438 -1 N GLU A 437 O VAL A 448 SHEET 1 AA8 2 ALA A 456 ILE A 458 0 SHEET 2 AA8 2 VAL A 464 ILE A 466 -1 O VAL A 465 N GLU A 457 SHEET 1 AA9 4 GLN H 3 SER H 7 0 SHEET 2 AA9 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA9 4 ASN H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA9 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AB1 6 LEU H 11 VAL H 12 0 SHEET 2 AB1 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB1 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AB1 6 MET H 34 GLN H 39 -1 N VAL H 37 O PHE H 91 SHEET 5 AB1 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AB1 6 THR H 57 TYR H 58 -1 O TYR H 58 N THR H 50 SHEET 1 AB2 4 LEU H 11 VAL H 12 0 SHEET 2 AB2 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB2 4 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AB2 4 TYR H 102 TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AB3 4 SER H 120 LEU H 124 0 SHEET 2 AB3 4 VAL H 136 TYR H 145 -1 O LEU H 141 N TYR H 122 SHEET 3 AB3 4 TYR H 175 VAL H 183 -1 O TYR H 175 N TYR H 145 SHEET 4 AB3 4 VAL H 163 THR H 165 -1 N HIS H 164 O SER H 180 SHEET 1 AB4 4 SER H 120 LEU H 124 0 SHEET 2 AB4 4 VAL H 136 TYR H 145 -1 O LEU H 141 N TYR H 122 SHEET 3 AB4 4 TYR H 175 VAL H 183 -1 O TYR H 175 N TYR H 145 SHEET 4 AB4 4 LEU H 169 LEU H 170 -1 N LEU H 169 O THR H 176 SHEET 1 AB5 3 THR H 151 TRP H 154 0 SHEET 2 AB5 3 THR H 194 HIS H 199 -1 O SER H 196 N THR H 153 SHEET 3 AB5 3 THR H 204 LYS H 209 -1 O VAL H 206 N VAL H 197 SHEET 1 AB6 4 SER L 5 SER L 7 0 SHEET 2 AB6 4 VAL L 19 ARG L 24 -1 O THR L 22 N SER L 7 SHEET 3 AB6 4 SER L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AB6 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB7 6 ILE L 10 LEU L 11 0 SHEET 2 AB7 6 THR L 102 LEU L 104 1 O LYS L 103 N LEU L 11 SHEET 3 AB7 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB7 6 HIS L 34 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AB7 6 LYS L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AB7 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AB8 4 ILE L 10 LEU L 11 0 SHEET 2 AB8 4 THR L 102 LEU L 104 1 O LYS L 103 N LEU L 11 SHEET 3 AB8 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB8 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB9 4 THR L 114 PHE L 118 0 SHEET 2 AB9 4 GLY L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AB9 4 TYR L 173 THR L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 AB9 4 LEU L 160 TRP L 163 -1 N LEU L 160 O THR L 178 SHEET 1 AC1 3 ASN L 145 LYS L 149 0 SHEET 2 AC1 3 TYR L 192 THR L 197 -1 O GLU L 195 N LYS L 147 SHEET 3 AC1 3 SER L 208 PHE L 209 -1 O PHE L 209 N TYR L 192 SSBOND 1 CYS A 94 CYS A 247 1555 1555 2.00 SSBOND 2 CYS A 162 CYS A 192 1555 1555 2.11 SSBOND 3 CYS A 208 CYS A 220 1555 1555 2.05 SSBOND 4 CYS A 265 CYS A 363 1555 1555 1.98 SSBOND 5 CYS A 282 CYS A 354 1555 1555 2.07 SSBOND 6 CYS A 388 CYS A 444 1555 1555 2.02 SSBOND 7 CYS A 432 CYS A 449 1555 1555 2.05 SSBOND 8 CYS A 434 CYS A 451 1555 1555 2.00 SSBOND 9 CYS H 22 CYS H 92 1555 1555 2.07 SSBOND 10 CYS H 140 CYS H 195 1555 1555 2.05 SSBOND 11 CYS L 23 CYS L 88 1555 1555 2.06 SSBOND 12 CYS L 134 CYS L 194 1555 1555 2.07 LINK C PCA L 1 N ILE L 2 1555 1555 1.39 CISPEP 1 SER A 136 PRO A 137 0 -11.29 CISPEP 2 PHE H 146 PRO H 147 0 -4.36 CISPEP 3 GLU H 148 SER H 149 0 3.93 CISPEP 4 TRP H 188 PRO H 189 0 -0.10 CISPEP 5 SER L 7 PRO L 8 0 -0.72 CISPEP 6 ASN L 94 PRO L 95 0 3.56 CISPEP 7 TYR L 140 PRO L 141 0 3.69 CRYST1 73.390 214.680 57.410 90.00 90.00 90.00 P 21 21 2 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.013626 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004658 0.000000 0.00000 SCALE3 0.000000 0.000000 0.017419 0.00000